Skip to Main content Skip to Navigation
Journal articles

Structure-function relationships of membrane-associated GT-B glycosyltransferases

Abstract : Membrane-associated GT-B glycosyltransferases (GTs) comprise a large family of enzymes that catalyze the transfer of a sugar moiety from nucleotide-sugar donors to a wide range of membrane-associated acceptor substrates, mostly in the form of lipids and proteins. As a consequence, they generate a significant and diverse amount of glycoconjugates in biological membranes, which are particularly important in cell-cell, cell-matrix and host-pathogen recognition events. Membrane-associated GT-B enzymes display two "Rossmann-fold" domains separated by a deep cleft that includes the catalytic center. They associate permanently or temporarily to the phospholipid bilayer by a combination of hydrophobic and electrostatic interactions. They have the remarkable property to access both hydrophobic and hydrophilic substrates that reside within chemically distinct environments catalyzing their enzymatic transformations in an efficient manner. Here, we discuss the considerable progress that has been made in recent years in understanding the molecular mechanism that governs substrate and membrane recognition, and the impact of the conformational transitions undergone by these GTs during the catalytic cycle.
Complete list of metadata

https://hal-pasteur.archives-ouvertes.fr/pasteur-03096123
Contributor : Marie de Tarragon <>
Submitted on : Monday, January 4, 2021 - 7:40:05 PM
Last modification on : Friday, January 22, 2021 - 3:26:58 AM

Links full text

Identifiers

Collections

Citation

David Albesa-Jove, David Giganti, Mary Jackson, Pedro Alzari, Marcelo Guerin. Structure-function relationships of membrane-associated GT-B glycosyltransferases. Glycobiology, Oxford University Press (OUP), 2014, 24 (2), pp.108-124. ⟨10.1093/glycob/cwt101⟩. ⟨pasteur-03096123⟩

Share

Metrics

Record views

49